Surfactant-Stabilized Protein Formulations: A Review of Protein-Surfactant Interactions and Novel Analytical Methodologies

Jones, LaToya S.; Bam, Narendra B.; Randolph, Theodore W.

doi:10.1021/bk-1997-0675.ch012

Cited by 44 publications

(36 citation statements)

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“…The binding of IgG1 to plastic has been reported (334), and BSA, like other proteins, exhibits some propensity to bind to stainless steel (335). Consequently, many biophysical studies have been published on protein adsorption, especially as it applies to processing and protein instability (336)(337)(338)(339)(340).…”

Section: Surface Adsorptionmentioning

confidence: 99%

Stability of Protein Pharmaceuticals: An Update

Manning¹,

Chou²,

Murphy³

et al. 2010

Pharm Res

986

782

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In 1989, Manning, Patel, and Borchardt wrote a review of protein stability (Manning et al., Pharm. Res. 6:903-918, 1989), which has been widely referenced ever since. At the time, recombinant protein therapy was still in its infancy. This review summarizes the advances that have been made since then regarding protein stabilization and formulation. In addition to a discussion of the current understanding of chemical and physical instability, sections are included on stabilization in aqueous solution and the dried state, the use of chemical modification and mutagenesis to improve stability, and the interrelationship between chemical and physical instability.

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Section: Surface Adsorptionmentioning

confidence: 99%

Stability of Protein Pharmaceuticals: An Update

Manning¹,

Chou²,

Murphy³

et al. 2010

Pharm Res

986

782

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show abstract

“…[10][11][12][13][14][19][20][21] These surfactants bind weakly to proteins and do not unfold or denature the protein even at moderate concentration. 10,20 -23 Polysorbate, pluronic, and other similar non-ionic surfactants have been studied for their ability to prevent adsorption of proteins to surfaces as well as their ability to inhibit protein denaturation, aggregation, and precipitation.…”

Section: Stabilizing Effect Of Non-ionic Surfactant On Hpv Vlpsmentioning

confidence: 99%

“…Physical factors can cause such protein denaturation in the absence of chemical denaturants. [10][11][12] These factors include heat stress, surface binding, and physical agitation such as stirring, shaking, and vortexing that can generate significant air/solution interfaces. 12,31,32 The interaction of proteins with solid surfaces and/or air/solution interfaces can result in denaturation or unfolding and eventual aggregation of proteins.…”

Section: Mechanisms Of Hpv Vlp Aggregationmentioning

confidence: 99%

“…[10][11][12][13][14] The study reported here shows that non-ionic surfactants in combination with electrolytes provide significant stabilization to HPV VLPs in solution allowing the VLPs to be handled under a variety of conditions without aggregation. The mechanism of HPV VLP stabilization by non-ionic surfactants has also been elucidated and is discussed as well.…”

Section: Introductionmentioning

confidence: 99%

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Stabilization of human papillomavirus virus-like particles by non-ionic surfactants

Shi

Sanyal

et al. 2005

Journal of Pharmaceutical Sciences

112

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“…Polysorbate 80 is widely used in protein formulations to prevent agitation-induced aggregation because of its effectiveness at low concentrations, relative low toxicity, and ability to not only inhibit protein surface adsorption and aggregation under various processing conditions but also act as a stabilizer against protein aggregation (4)(5)(6). Although nonionic surfactants like Polysorbates 80 and 20 are used extensively, mechanisms by which they provide stabilizing effects are only fairly understood (7). Several mechanisms for protein stabilization by surfactants have been reported in the literature.…”

Section: Introductionmentioning

confidence: 99%

Effect of Polysorbate 80 Concentration on Thermal and Photostability of a Monoclonal Antibody

et al. 2012

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Abstract. Polysorbate 80 is widely used in protein formulations to protect protein against agitationinduced aggregation. In this study, we address concerns about residual peroxide present in Polysorbate 80 on protein stability. Residual peroxide may oxidize active pharmaceutical ingredients leading to reduced stability and may ultimately lead to lower potency and efficacy. The effect of Polysorbate 80 concentration on thermal and photostability of monoclonal antibody of the IgG1 subclass (MAb1) was evaluated at Polysorbate 80 concentrations ranging from 0.00% to 1.00% (w/v). MAb1 samples at 5 mg/ mL with various Polysorbate 80 concentrations were subjected to accelerated thermal stress by incubation at 25°C, 40°C, and 50°C for a period of 4 weeks and light stress per ICH guideline Q1B, option 1. Our results show that Polysorbate 80 concentration of 1.00% (w/v) adversely affected thermal and photostability of MAb1. This study demonstrates the importance of carefully choosing Polysorbate 80 concentration in protein formulations to prevent destabilizing effect of Polysorbate 80 on thermal and photostability.

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Surfactant-Stabilized Protein Formulations: A Review of Protein-Surfactant Interactions and Novel Analytical Methodologies

Cited by 44 publications

References 0 publications

Stability of Protein Pharmaceuticals: An Update

Stability of Protein Pharmaceuticals: An Update

Stabilization of human papillomavirus virus-like particles by non-ionic surfactants

Effect of Polysorbate 80 Concentration on Thermal and Photostability of a Monoclonal Antibody

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